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Volumn 166, Issue 2, 2009, Pages 214-225

On the quaternary association of the type III secretion system HrcQB-C protein: Experimental evidence differentiates among the various oligomerization models

Author keywords

Circular dichroism (CD); FliN protein; Plant pathogens; Protein oligomerization state; Small angle X ray scattering (SAXS)

Indexed keywords

BACTERIAL PROTEIN; GLUTARALDEHYDE; TETRAMER;

EID: 63649127135     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2009.01.008     Document Type: Article
Times cited : (10)

References (46)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 2
    • 16844367441 scopus 로고    scopus 로고
    • Crystal structure of the flagellar rotor protein FliN from Thermotoga maritima
    • Brown P.N., Mathews M.A.A., Joss L.A., Hill C.P., and Blair D.F. Crystal structure of the flagellar rotor protein FliN from Thermotoga maritima. J. Bacteriol. 187 (2005) 2890-2902
    • (2005) J. Bacteriol. , vol.187 , pp. 2890-2902
    • Brown, P.N.1    Mathews, M.A.A.2    Joss, L.A.3    Hill, C.P.4    Blair, D.F.5
  • 3
    • 63649105295 scopus 로고    scopus 로고
    • Brünger, A.T, 1992. X-PLOR, version 3.1
    • Brünger, A.T., 1992. X-PLOR, version 3.1.
  • 4
    • 0036532450 scopus 로고    scopus 로고
    • Port of entry-the type III secretion translocon
    • Buttner D., and Bonas U. Port of entry-the type III secretion translocon. Trends Microbiol. 10 (2002) 186-192
    • (2002) Trends Microbiol. , vol.10 , pp. 186-192
    • Buttner, D.1    Bonas, U.2
  • 5
    • 0042071205 scopus 로고    scopus 로고
    • Common infection strategies of plant and animal pathogenic bacteria
    • Buttner D., and Bonas U. Common infection strategies of plant and animal pathogenic bacteria. Curr. Opin. Plant Biol. 6 (2003) 312-319
    • (2003) Curr. Opin. Plant Biol. , vol.6 , pp. 312-319
    • Buttner, D.1    Bonas, U.2
  • 6
    • 33846823909 scopus 로고
    • Particle mesh Ewald. An N log(N) method for Ewald sums in large systems
    • Darden T., York D., and Pedersen L. Particle mesh Ewald. An N log(N) method for Ewald sums in large systems. J. Chem. Phys. 98 (1993) 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 7
    • 37649022489 scopus 로고    scopus 로고
    • Determination of protein oligomerization state: two approaches based on glutaraldehyde crosslinking
    • Fadouloglou V.E., Kokkinidis M., and Glykos N.M. Determination of protein oligomerization state: two approaches based on glutaraldehyde crosslinking. Anal. Biochem. 373 (2008) 404-406
    • (2008) Anal. Biochem. , vol.373 , pp. 404-406
    • Fadouloglou, V.E.1    Kokkinidis, M.2    Glykos, N.M.3
  • 11
    • 0343471377 scopus 로고    scopus 로고
    • Modification of a PCR-based site-directed mutagenesis method
    • Fisher C., and Pei G.K. Modification of a PCR-based site-directed mutagenesis method. Biotechniques 23 (1997) 570-574
    • (1997) Biotechniques , vol.23 , pp. 570-574
    • Fisher, C.1    Pei, G.K.2
  • 12
    • 0028274712 scopus 로고
    • Isolation, characterization and structure of bacterial flagellar motors containing the switch complex
    • Francis N.R., Sosinsky G.E., Thomas D., and DeRosier D.J. Isolation, characterization and structure of bacterial flagellar motors containing the switch complex. J. Mol. Biol. 235 (1994) 1261-1270
    • (1994) J. Mol. Biol. , vol.235 , pp. 1261-1270
    • Francis, N.R.1    Sosinsky, G.E.2    Thomas, D.3    DeRosier, D.J.4
  • 13
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • García-de-la-Torre J., Huertas M.L., and Carrasco B. Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 78 (2000) 719-730
    • (2000) Biophys. J. , vol.78 , pp. 719-730
    • García-de-la-Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 14
    • 0038242826 scopus 로고    scopus 로고
    • Resolving near-ultraviolet circular dichroism spectra of single trp mutants in tear lipocalin
    • Gasymov O.K., Abduragimov A.R., Yusifov T.N., and Glasgow B.J. Resolving near-ultraviolet circular dichroism spectra of single trp mutants in tear lipocalin. Anal. Biochem. 318 (2003) 300-308
    • (2003) Anal. Biochem. , vol.318 , pp. 300-308
    • Gasymov, O.K.1    Abduragimov, A.R.2    Yusifov, T.N.3    Glasgow, B.J.4
  • 15
    • 33749172039 scopus 로고    scopus 로고
    • Carma: a molecular dynamics analysis program
    • Glykos N.M. Carma: a molecular dynamics analysis program. J. Comput. Chem. 27 (2006) 1765-1768
    • (2006) J. Comput. Chem. , vol.27 , pp. 1765-1768
    • Glykos, N.M.1
  • 16
    • 0001498978 scopus 로고
    • La diffraction des rayons X aux très petits angles; application a l'étude de phenomenes ultramicroscopiques
    • Guinier A. La diffraction des rayons X aux très petits angles; application a l'étude de phenomenes ultramicroscopiques. Ann. Phys. (Paris) 12 (1939) 161-237
    • (1939) Ann. Phys. (Paris) , vol.12 , pp. 161-237
    • Guinier, A.1
  • 17
    • 0019074582 scopus 로고
    • Electrostatic stabilization in sperm whale and harbor seal myoglobins. Identification of groups primarily responsible for changes in anchoring of the A helix
    • Gurd F.R.N., Friend S.H., Rothgeb T.M., Gurd R.S., and Scouloudi H. Electrostatic stabilization in sperm whale and harbor seal myoglobins. Identification of groups primarily responsible for changes in anchoring of the A helix. Biophys. J. 32 (1980) 65-75
    • (1980) Biophys. J. , vol.32 , pp. 65-75
    • Gurd, F.R.N.1    Friend, S.H.2    Rothgeb, T.M.3    Gurd, R.S.4    Scouloudi, H.5
  • 18
    • 0037325044 scopus 로고    scopus 로고
    • The Hrp pilus: learning from flagella
    • He S.Y., and Jin Q. The Hrp pilus: learning from flagella. Curr. Opin. Microbiol. 6 (2003) 15-19
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 15-19
    • He, S.Y.1    Jin, Q.2
  • 19
    • 0031864184 scopus 로고    scopus 로고
    • Type III protein secretion systems in bacterial pathogens of animals and plants
    • Hueck C.J. Type III protein secretion systems in bacterial pathogens of animals and plants. Microbiol. Mol. Biol. Rev. 62 (1998) 379-433
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 379-433
    • Hueck, C.J.1
  • 22
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch W. A solution for the best rotation to relate two sets of vectors. Acta Crystallogr. A 32 (1978) 922-923
    • (1978) Acta Crystallogr. A , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 25
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin M.B., and Svergun D.I. Automated matching of high- and low-resolution structural models. J. Appl. Crystallogr. 34 (2001) 33-41
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 29
    • 0031771710 scopus 로고    scopus 로고
    • Domain analysis of the FliM protein of Escherichia coli
    • Mathews M.A., Tang H.L., and Blair D.F. Domain analysis of the FliM protein of Escherichia coli. J. Bacteriol. 180 (1998) 5580-5590
    • (1998) J. Bacteriol. , vol.180 , pp. 5580-5590
    • Mathews, M.A.1    Tang, H.L.2    Blair, D.F.3
  • 31
    • 33645233315 scopus 로고    scopus 로고
    • Organization of FliN subunits in the flagellar motor of Escherichia coli
    • Paul K., and Blair D.F. Organization of FliN subunits in the flagellar motor of Escherichia coli. J. Bacteriol. 188 (2006) 2502-2511
    • (2006) J. Bacteriol. , vol.188 , pp. 2502-2511
    • Paul, K.1    Blair, D.F.2
  • 32
    • 0015767025 scopus 로고
    • Polymerization of proteins with glutaraldehyde
    • Payne J.W. Polymerization of proteins with glutaraldehyde. Biochem. J. 153 (1973) 867-873
    • (1973) Biochem. J. , vol.153 , pp. 867-873
    • Payne, J.W.1
  • 33
    • 0014690666 scopus 로고
    • Optical activity of cystine-containing proteins. II. Circular dichroism spectra of pancreatic ribonuclease A, ribonuclease S, and ribonuclease S-protein
    • Pflumm M.N., and Beychok S. Optical activity of cystine-containing proteins. II. Circular dichroism spectra of pancreatic ribonuclease A, ribonuclease S, and ribonuclease S-protein. J. Biol. Chem. 244 (1969) 3973-3981
    • (1969) J. Biol. Chem. , vol.244 , pp. 3973-3981
    • Pflumm, M.N.1    Beychok, S.2
  • 34
    • 0033529826 scopus 로고    scopus 로고
    • The Xanthomonas Hrp type III system secretes proteins from plant and animal bacterial pathogens
    • Rossier O., Wengelnik K., Hahn K., and Bonas U. The Xanthomonas Hrp type III system secretes proteins from plant and animal bacterial pathogens. Proc. Natl. Acad. Sci. USA 96 (1999) 9368-9373
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9368-9373
    • Rossier, O.1    Wengelnik, K.2    Hahn, K.3    Bonas, U.4
  • 35
    • 0035949491 scopus 로고    scopus 로고
    • Supermolecular structure of the enteropathogenic Escherichia coli type III secretion system and its direct interaction with the EspA-sheath-like structure
    • Sekiya K., Ohishi M., Ogino T., Tamano K., Sasakawa C., and Abe A. Supermolecular structure of the enteropathogenic Escherichia coli type III secretion system and its direct interaction with the EspA-sheath-like structure. Proc. Natl. Acad. Sci. USA 98 (2001) 11638-11643
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11638-11643
    • Sekiya, K.1    Ohishi, M.2    Ogino, T.3    Tamano, K.4    Sasakawa, C.5    Abe, A.6
  • 37
    • 0014559763 scopus 로고
    • Fine structure in the near-ultraviolet circular dichroism and absorption spectra of tryptophan derivatives and chymotrypsinogen A at 77 degrees K
    • Strickland E.H., Horwitz J., and Billups C. Fine structure in the near-ultraviolet circular dichroism and absorption spectra of tryptophan derivatives and chymotrypsinogen A at 77 degrees K. Biochemistry 8 (1969) 3205-3213
    • (1969) Biochemistry , vol.8 , pp. 3205-3213
    • Strickland, E.H.1    Horwitz, J.2    Billups, C.3
  • 38
    • 0015236372 scopus 로고
    • Near-ultraviolet absorption bands of tryptophan. Studies using horseradish peroxidase isoenzymes, bovine and horse heart cytochrome c, and N-stearyl-l-tryptophan n-hexyl ester
    • Strickland E.H., Horwitz J., Kay E., Shannon L.M., Wilchek M., and Billups C. Near-ultraviolet absorption bands of tryptophan. Studies using horseradish peroxidase isoenzymes, bovine and horse heart cytochrome c, and N-stearyl-l-tryptophan n-hexyl ester. Biochemistry 10 (1971) 2631-2638
    • (1971) Biochemistry , vol.10 , pp. 2631-2638
    • Strickland, E.H.1    Horwitz, J.2    Kay, E.3    Shannon, L.M.4    Wilchek, M.5    Billups, C.6
  • 39
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun D.I. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25 (1992) 495-503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 40
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun D.I. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76 (1999) 2879-2886
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 41
    • 0029185933 scopus 로고
    • CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D.I., Barberato C., and Koch M.H.J. CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28 (1995) 768-773
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 42
    • 0034254475 scopus 로고    scopus 로고
    • Supramolecular structure of the Shigella type III secretion machinery: the needle part is changeable in length and essential for delivery of effectors
    • Tamano K., Aizawa S.-I., Katayama E., Nonaka T., Imajoh-Ohmi S., Kuwae A., Nagai S., and Sasakawa C. Supramolecular structure of the Shigella type III secretion machinery: the needle part is changeable in length and essential for delivery of effectors. EMBO J. 19 (2000) 3876-3887
    • (2000) EMBO J. , vol.19 , pp. 3876-3887
    • Tamano, K.1    Aizawa, S.-I.2    Katayama, E.3    Nonaka, T.4    Imajoh-Ohmi, S.5    Kuwae, A.6    Nagai, S.7    Sasakawa, C.8
  • 44
    • 0029009964 scopus 로고
    • Regulated underexpression and overexpression of the FliN protein of Escherichia coli and evidence for an interaction between FliN and FliM in the flagellar motor
    • Tang H., Billings S., Wang X., Sharp L., and Blair D.F. Regulated underexpression and overexpression of the FliN protein of Escherichia coli and evidence for an interaction between FliN and FliM in the flagellar motor. J. Bacteriol. 177 (1995) 3496-3503
    • (1995) J. Bacteriol. , vol.177 , pp. 3496-3503
    • Tang, H.1    Billings, S.2    Wang, X.3    Sharp, L.4    Blair, D.F.5
  • 45
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov V.V., and Svergun D.I. Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 36 (2003) 860-864
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 46
    • 0030590265 scopus 로고    scopus 로고
    • FliN is a major structural protein of the C-ring in the Salmonella typhimurium flagellar basal body
    • Zhao R., Pathak N., Jaffe H., Reese T.S., and Khan S. FliN is a major structural protein of the C-ring in the Salmonella typhimurium flagellar basal body. J. Mol. Biol. 261 (1996) 195-208
    • (1996) J. Mol. Biol. , vol.261 , pp. 195-208
    • Zhao, R.1    Pathak, N.2    Jaffe, H.3    Reese, T.S.4    Khan, S.5


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